D3321
Dipeptidyl Peptidase VII human
recombinant, expressed in Sf9 cells
Synonym(s):
DPP7, Quiescent cell proline dipeptidase
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About This Item
Enzyme Commission number:
3.4.14.-
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
recombinant
expressed in Sf9 cells
Quality Level
form
solution
specific activity
≥1,500 units/μg protein
≥1500 units/μg protein
mol wt
89.1 kDa
relevant disease(s)
diabetes; cardiovascular diseases
shipped in
dry ice
storage temp.
−70°C
Application
Dipeptidyl Peptidase VII (DPP7), also known as DPP2 or quiescent cell proline dipeptidase, is a post-proline cleaving aminopeptidase that is expressed in quiescent lymphocytes . DPP7 is used to study the regulation of cell quiescence . Like DPP4, DPP7 may be useful in diabetes and vascular disease research .
Biochem/physiol Actions
DPP7 is essential for maintaining lymphocytes and fibroblasts in G(0). The inhibition of DPP7 results in apoptosis, which is mediated by the induction of c-Myc and p53 . DPP7 has strong sequence homology with prolylcarboxypeptidase and is active at both acidic and neutral pH.
Physical properties
Contains amino acids 29 to end with a C-terminal His tag, MW=89.1 kDa
Unit Definition
One unit will hydrolyze 1.0 picomole of Ala-Pro-AMC per minute at pH 7.4 at 25 deg °C
Physical form
Supplied as a solution in 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 220 mM imidazole, and 20% glycerol.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Dam. 1 - Repr. 1B - Skin Corr. 1C
Storage Class Code
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
WGK
WGK 2
Certificates of Analysis (COA)
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Dolan Sondhi et al.
Human gene therapy methods, 23(5), 324-335 (2012-11-08)
Late infantile neuronal ceroid lipofuscinosis (LINCL), a fatal, lysosomal storage disorder caused by mutations in the CLN2 gene, results in a deficiency of tripeptidyl-peptidase I (TPP-I) activity in neurons. Our prior studies showed that delivery of the human CLN2 cDNA
Wengen Wu et al.
Bioorganic & medicinal chemistry letters, 22(17), 5536-5540 (2012-08-03)
The boroProline-based dipeptidyl boronic acids were among the first DPP-IV inhibitors identified, and remain the most potent known. We introduced various substitutions at the 4-position of the boroProline ring regioselectively and stereoselectively, and incorporated these aminoboronic acids into a series
Helen Hwang et al.
Structure (London, England : 1993), 20(11), 1872-1880 (2012-09-18)
Human telomeres possess a single-stranded DNA (ssDNA) overhang of TTAGGG repeats, which can self-fold into a G-quadruplex structure. POT1 binds specifically to the telomeric overhang and partners with TPP1 to regulate telomere lengthening and capping, although the mechanism remains elusive.
Brian D Green et al.
Diabetes & vascular disease research, 3(3), 159-165 (2006-12-13)
Inhibitors of the enzyme dipeptidyl peptidase IV (DPP IV) provide a strategy for the treatment of type 2 diabetes. DPP IV rapidly inactivates the incretin hormones glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP). Inhibition of DPP IV prolongs and
Martin Kruse et al.
The Journal of general physiology, 140(2), 189-205 (2012-08-02)
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) regulates activities of numerous ion channels including inwardly rectifying potassium (K(ir)) channels, KCNQ, TRP, and voltage-gated calcium channels. Several studies suggest that voltage-gated potassium (K(V)) channels might be regulated by PI(4,5)P(2). Wide expression of K(V) channels in
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